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Gene Review

Enah  -  enabled homolog (Drosophila)

Mus musculus

Synonyms: AI464316, AW045240, Mena, NDPP-1, NPC-derived proline-rich protein 1, ...
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Disease relevance of Enah


Psychiatry related information on Enah

  • Further characterization of the FE65-Mena complex may identify a physiological role for these proteins in beta-amyloid precursor protein biogenesis and may help in understanding the mechanism of molecular changes that underlie Alzheimer disease [5].

High impact information on Enah

  • In keratinocytes either null for alpha-catenin or blocked in VASP/Mena function, filopodia embed, but actin reorganization/polymerization is prevented, and membranes cannot seal [6].
  • The crystal structure of the mammalian Enabled (Mena) EVH1 domain complexed with a peptide ligand reveals a mechanism of recognition distinct from that used by other proline-binding modules [7].
  • Expression of neural-enriched isoforms of Mena in fibroblasts induces the formation of abnormal F-actin-rich outgrowths, supporting a role for this protein in microfilament assembly and cell motility [1].
  • In primary neurons, Mena is concentrated at the tips of growth cone filopodia [8].
  • Mammalian enabled (Mena) is a member of a protein family thought to link signal transduction pathways to localized remodeling of the actin cytoskeleton [8].

Biological context of Enah


Anatomical context of Enah


Associations of Enah with chemical compounds

  • Fat was shown to be significantly downregulated (P=0.027), and Catnb and Enah were significantly upregulated (P=0.0003 and 0.005, respectively), in response to therapeutic doses of lithium [13].
  • Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalian enabled (Mena) by c-Abl kinase [10].
  • The stimulatory effect of misonidazole and NDPP on O2 utilization in medium with glucose undoubtedly appeared as a release from the Crabtree effect [4].
  • A stimulatory effect on O2 consumption was found for 5--20mM misonidazole as well as for 0.5mM NDPP, both in media containing 10(-2)M glucose [4].

Physical interactions of Enah


Other interactions of Enah

  • In this study, we investigated the consequence of deleting both Mena and VASP [9].
  • Our functional data, substantiated by structural data, demonstrate that the ligand-binding of the Vesl EVH1 domain differs from the interaction characteristics of the previously examined EVH1 domains of the Evl/Mena proteins [14].
  • IRSp53 is colocalised with WAVE2 at the tips of protruding lamellipodia and filopodia independently of Mena [15].
  • VASP and Mena immunoreactivity in heart is associated with blood vessels and with the intercalated discs of cardiac myocytes, where they colocalize with connexin-43 [12].

Analytical, diagnostic and therapeutic context of Enah


  1. Mena, a relative of VASP and Drosophila Enabled, is implicated in the control of microfilament dynamics. Gertler, F.B., Niebuhr, K., Reinhard, M., Wehland, J., Soriano, P. Cell (1996) [Pubmed]
  2. Accumulation of profilin II at the surface of Listeria is concomitant with the onset of motility and correlates with bacterial speed. Geese, M., Schlüter, K., Rothkegel, M., Jockusch, B.M., Wehland, J., Sechi, A.S. J. Cell. Sci. (2000) [Pubmed]
  3. Identification of a developmentally regulated gene in the mouse central nervous system which encodes a novel proline rich protein. Sazuka, T., Tomooka, Y., Kathju, S., Ikawa, Y., Noda, M., Kumar, S. Biochim. Biophys. Acta (1992) [Pubmed]
  4. Release from the Crabtree effect by hypoxic cell radiosensitizers. Mustea, I., Bara, A. Br. J. Cancer (1979) [Pubmed]
  5. The WW domain of neural protein FE65 interacts with proline-rich motifs in Mena, the mammalian homolog of Drosophila enabled. Ermekova, K.S., Zambrano, N., Linn, H., Minopoli, G., Gertler, F., Russo, T., Sudol, M. J. Biol. Chem. (1997) [Pubmed]
  6. Directed actin polymerization is the driving force for epithelial cell-cell adhesion. Vasioukhin, V., Bauer, C., Yin, M., Fuchs, E. Cell (2000) [Pubmed]
  7. Structure of the enabled/VASP homology 1 domain-peptide complex: a key component in the spatial control of actin assembly. Prehoda, K.E., Lee, D.J., Lim, W.A. Cell (1999) [Pubmed]
  8. Mena is required for neurulation and commissure formation. Lanier, L.M., Gates, M.A., Witke, W., Menzies, A.S., Wehman, A.M., Macklis, J.D., Kwiatkowski, D., Soriano, P., Gertler, F.B. Neuron (1999) [Pubmed]
  9. Mena and vasodilator-stimulated phosphoprotein are required for multiple actin-dependent processes that shape the vertebrate nervous system. Menzies, A.S., Aszodi, A., Williams, S.E., Pfeifer, A., Wehman, A.M., Goh, K.L., Mason, C.A., Fassler, R., Gertler, F.B. J. Neurosci. (2004) [Pubmed]
  10. Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalian enabled (Mena) by c-Abl kinase. Tani, K., Sato, S., Sukezane, T., Kojima, H., Hirose, H., Hanafusa, H., Shishido, T. J. Biol. Chem. (2003) [Pubmed]
  11. Critical roles of phosphorylation and actin binding motifs, but not the central proline-rich region, for Ena/vasodilator-stimulated phosphoprotein (VASP) function during cell migration. Loureiro, J.J., Rubinson, D.A., Bear, J.E., Baltus, G.A., Kwiatkowski, A.V., Gertler, F.B. Mol. Biol. Cell (2002) [Pubmed]
  12. Distribution, cellular localization, and postnatal development of VASP and Mena expression in mouse tissues. Gambaryan, S., Hauser, W., Kobsar, A., Glazova, M., Walter, U. Histochem. Cell Biol. (2001) [Pubmed]
  13. Positional cloning, association analysis and expression studies provide convergent evidence that the cadherin gene FAT contains a bipolar disorder susceptibility allele. Blair, I.P., Chetcuti, A.F., Badenhop, R.F., Scimone, A., Moses, M.J., Adams, L.J., Craddock, N., Green, E., Kirov, G., Owen, M.J., Kwok, J.B., Donald, J.A., Mitchell, P.B., Schofield, P.R. Mol. Psychiatry (2006) [Pubmed]
  14. The N-terminal domain of Homer/Vesl is a new class II EVH1 domain. Barzik, M., Carl, U.D., Schubert, W.D., Frank, R., Wehland, J., Heinz, D.W. J. Mol. Biol. (2001) [Pubmed]
  15. IRSp53 is colocalised with WAVE2 at the tips of protruding lamellipodia and filopodia independently of Mena. Nakagawa, H., Miki, H., Nozumi, M., Takenawa, T., Miyamoto, S., Wehland, J., Small, J.V. J. Cell. Sci. (2003) [Pubmed]
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